Asialofetuin에 대한 Aspergillus oryzae, bovine liver, Saccharomyces fragilis 유래 beta-galactosidase의 반응 조건

• 영문명: The Reaction Conditions of beta-Galactosidases from Aspergillus oryzae, Bovine Liver, and Saccharomyces fragilis to Asialofetuin
• 발행기관: 대한약학회
• 저자명: 윤재경(Jae Kyoung Youn) 이영재(Young Jae Lee) 구본웅(Bon Woong Koo) 윤상영(Sang Young Youn) 유창수(Chang Soo Ryu) 김하형(Ha Hyung Kim)
• 간행물 정보: 『약학회지』제44권 제2호 (2000년), 197~203쪽, 전체 7쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 2000.04.29

영문 초록

The enzymatic properties of beta-galactosidases from Aspergillus oryzae, bovine liver and Saccharomyces fragilis have been studied using enzyme-linked lectin assay based on the RCA120 and BS-II lectins which specifically bind to terminal galactose and G1cNAc residue, respectively. Asialofetuin, a monomeric glycoprotein with approximately 48kDa in molecular weight, was used as a substrate. This glycoprotein contains three N-linked triantennary complex type carbohydrate chains with each of which terminating in Ga1beta1-4GlcNAc (74%). Their optimal pHs were 3.5 and 6.5 (A. oryzae), and 3.5~5.5 (bovine liver and S.fragilis) at 37oC during 24hrs, and the effective concentrations were 0.9, 2.9, and 1.7mg/ml, respectively. The enzyme from A.oryzae requires 100mM Na+ or K+, while the enzyme from bovine liver requires Ba2+ for activity. However all of the three beta-galactosidases were inactivated by SDS and CU2+. These results indicate that the hydrolysis of glycoprotein such as asialofetuin depends on the reaction conditions of beta-galactosidases and some metal ions.

키워드

β-galactosidase activity asialofetuin lectin.